Recombinant B. pertussis Adenylate Cyclase Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 8270-AC

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8270-AC-050
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Key Product Details

  • R&D Systems E. coli-derived Recombinant B. pertussis Adenylate Cyclase Protein (8270-AC)
  • Quality control testing to verify active proteins with lot specific assays by in-house scientists
  • All R&D Systems proteins are covered with a 100% guarantee

Source

E. coli

Accession #

P15318

Conjugate

Unconjugated

Applications

Enzyme Activity

View all Adenylate Cyclase Proteins and Enzymes »

Product Specifications

Source

E. coli-derived b. pertussis Adenylate Cyclase protein
Gln2-Arg399, with an N-terminal Met and 6-His tag

Purity

>90%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain at 5 μg per lane.

Endotoxin Level

<0.01 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Met

Predicted Molecular Mass

44 kDa

SDS-PAGE

42 kDa, reducing conditions

Activity

Measured by its ability to convert ATP to cAMP and pyrophosphate.
The specific activity is >250 nmol/min/μg, as measured under the described conditions.

Formulation, Preparation and Storage

8270-AC
Formulation Supplied as a 0.2 μm filtered solution in Tris and NaCl.
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.

Background: Adenylate Cyclase

B. pertussis Adenylate Cyclase is an enzymatic toxin that converts ATP to 3’-5’cyclic AMP and plays a role in the pathogenesis of whooping cough (1). The Km for ATP of the enzyme is 0.6 mM (2). The enzyme activity is calmodulin (CaM) dependent with a Kd for CaM of 0.2 nM. The protein is synthesized as a large bifunctional precursor of 1706 amino acid residues, endowed with Adenylate Cyclase and haemolytic activity (3). The enzyme corresponds to amino acid 1 to 399 and is released from the precursor as a 43 kD fragment. The N-terminal portion (residues 1-235/237) harbors the catalytic site, whereas the C-terminal portion (residues 235/237-399) corresponds to the main CaM-binding domain of the enzyme (4).

References

  1. Weiss, A.A. and E.L Hewlett (1986) Annu. Rev. Microbiol. 40:661.
  2. Glaser, P. et al. (1989) EMBO J.8:967.
  3. Shattuck, R.L. et al. (1985) Biochemistry 24:6358.
  4. Ladant, D. et al. (1989) J. Biol. Chem. 264: 4015.

UniProt

P15318

Additional Adenylate Cyclase Products

Product Documents for Recombinant B. pertussis Adenylate Cyclase Protein, CF

Product Datasheets

Certificate of Analysis

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Product Specific Notices for Recombinant B. pertussis Adenylate Cyclase Protein, CF

For research use only

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